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Specificity of binding of β-glucoside activators of ryegrass (1->3)-β-glucan synthase and the synthesis of some potential photoaffinity activators

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Version 1 2019-04-05, 18:25
journal contribution
posted on 2024-06-04, 02:58 authored by K Ng, Liz JohnsonLiz Johnson, BA Stone
Structure-activity relationships among glycoside activators of ryegrass (Lolium multiflorum) (1-->3)-beta-glucan synthase were investigated using a number of natural and synthetic glycosides, including some carrying photoaffinity functions. There is an absolute requirement for a beta-D-glycosyl moiety in the activator, both S- and N-glucosides are active, and the position of the glucosidic linkage in beta-glucose disaccharides has a significant effect on the affinity of binding. However, the binding requirement does not extend beyond a single beta-D-glucosyl residue, and beta-D-oligoglucosides are less effective than disaccharides. The nature of the aglycon has a major influence on the binding affinity. Hydrophobic aglycons lower the concentration required for half-maximal stimulation of the enzyme obtained from an Eadie-Hofstee plot of kinetic data (Ka) for activation, but charge aglycons increase Ka. Relative to methyl-beta-D-glucoside and cellobiose (Ka 1.1 mM), the most potent compounds tested were N-[4-(benzoyl)benzoyl]-beta-D-glucosylamine and 2'-[4-azidosalicylamino]ethyl-1-thio-beta-D-glucoside with K(a)s of approximately 30 microM. The latter also was tested for its potential to specifically label the beta-glucoside-binding site on the synthase, but under the conditions used the binding was found to be nonspecific.

History

Journal

Plant physiology

Volume

111

Pagination

1227-1231

Location

Rockville, Md.

Open access

  • Yes

ISSN

0032-0889

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

1996, American Society of Plant Biologists

Issue

4

Publisher

American Society of Plant Biologists

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